位置:首页 > 蛋白库 > CDN11_RANGI
CDN11_RANGI
ID   CDN11_RANGI             Reviewed;          12 AA.
AC   P62566; P56245; P81253;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   10-FEB-2021, entry version 29.
DE   RecName: Full=Caeridin-1.1/1.2/1.3;
OS   Ranoidea gilleni (Centralian tree frog) (Litoria gilleni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=39405;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-12, AND MASS SPECTROMETRY.
RC   TISSUE=Parotoid gland;
RA   Waugh R.J., Stone D.J.M., Bowie J.H., Wallace J.C., Tyler M.J.;
RT   "Peptides from Australian frogs. The structures of the caerins and
RT   caeridins from Litoria gilleni.";
RL   J. Chem. Res. 139:937-961(1993).
RN   [2]
RP   PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA   Waugh R.J., Steinborner S.T., Bowie J.H., Wallace J.C., Tyler M.J., Hu P.,
RA   Gross M.L.;
RT   "Two isomeric alpha and beta aspartyl dodecapeptides and their cyclic amino
RT   succinyl analogue from the Australian tree frog Litoria gilleni.";
RL   Aust. J. Chem. 48:1981-1987(1995).
CC   -!- FUNCTION: Caeridins show neither neuropeptide activity nor antibiotic
CC       activity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin parotoid and/or rostral
CC       glands.
CC   -!- PTM: Isomerization alpha-beta of the Asp-4 residue in caeridin 1.2; a
CC       cyclic succinimide may be formed between Asp-4 and Gly-5 residues in
CC       caeridin 1.3.
CC   -!- MASS SPECTROMETRY: Mass=1140; Method=FAB; Evidence={ECO:0000269|Ref.1};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Direct protein sequencing; Secreted.
FT   PEPTIDE         1..12
FT                   /note="Caeridin-1.1/1.2/1.3"
FT                   /id="PRO_0000043756"
FT   MOD_RES         12
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   12 AA;  1141 MW;  2822551A33772728 CRC64;
     GLLDGLLGTL GL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025